Pyranosone dehydratase from the basidiomycete Phanerochaete chrysosporium: improved purification, and identification of 6-deoxy-D-glucosone and D-xylosone reaction products.
Identifieur interne : 000D87 ( Main/Exploration ); précédent : 000D86; suivant : 000D88Pyranosone dehydratase from the basidiomycete Phanerochaete chrysosporium: improved purification, and identification of 6-deoxy-D-glucosone and D-xylosone reaction products.
Auteurs : J. Gabriel [République tchèque] ; J. Volc ; P. Sedmera ; G. Daniel ; E. KubátováSource :
- Archives of microbiology [ 0302-8933 ] ; 1993.
Descripteurs français
- KwdFr :
- Basidiomycota (enzymologie), Carbohydrate dehydrogenases (biosynthèse), Chromatographie d'échange d'ions (MeSH), Chélateurs (pharmacologie), Concentration en ions d'hydrogène (MeSH), Cétoses (sucres) (biosynthèse), Cétoses (sucres) (métabolisme), Désoxyglucose (analogues et dérivés), Désoxyglucose (biosynthèse), Désoxyglucose (métabolisme), Focalisation isoélectrique (MeSH), Hydro-lyases (biosynthèse), Hydro-lyases (composition chimique), Hydro-lyases (isolement et purification), Hydro-lyases (métabolisme), Spécificité du substrat (MeSH), Stabilité enzymatique (MeSH), Température élevée (MeSH), Électrophorèse sur gel de polyacrylamide (MeSH).
- MESH :
- analogues et dérivés : Désoxyglucose.
- biosynthèse : Carbohydrate dehydrogenases, Cétoses (sucres), Désoxyglucose, Hydro-lyases.
- composition chimique : Hydro-lyases.
- enzymologie : Basidiomycota.
- isolement et purification : Hydro-lyases.
- métabolisme : Cétoses (sucres), Désoxyglucose, Hydro-lyases.
- pharmacologie : Chélateurs.
- Chromatographie d'échange d'ions, Concentration en ions d'hydrogène, Focalisation isoélectrique, Spécificité du substrat, Stabilité enzymatique, Température élevée, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Basidiomycota (enzymology), Carbohydrate Dehydrogenases (biosynthesis), Chelating Agents (pharmacology), Chromatography, Ion Exchange (MeSH), Deoxyglucose (analogs & derivatives), Deoxyglucose (biosynthesis), Deoxyglucose (metabolism), Electrophoresis, Polyacrylamide Gel (MeSH), Enzyme Stability (MeSH), Hot Temperature (MeSH), Hydro-Lyases (biosynthesis), Hydro-Lyases (chemistry), Hydro-Lyases (isolation & purification), Hydro-Lyases (metabolism), Hydrogen-Ion Concentration (MeSH), Isoelectric Focusing (MeSH), Ketoses (biosynthesis), Ketoses (metabolism), Substrate Specificity (MeSH).
- MESH :
- chemical , analogs & derivatives : Deoxyglucose.
- chemical , biosynthesis : Carbohydrate Dehydrogenases, Deoxyglucose, Hydro-Lyases, Ketoses.
- chemical , chemistry : Hydro-Lyases.
- enzymology : Basidiomycota.
- chemical , isolation & purification : Hydro-Lyases.
- chemical , metabolism : Deoxyglucose, Hydro-Lyases, Ketoses.
- chemical , pharmacology : Chelating Agents.
- Chromatography, Ion Exchange, Electrophoresis, Polyacrylamide Gel, Enzyme Stability, Hot Temperature, Hydrogen-Ion Concentration, Isoelectric Focusing, Substrate Specificity.
Abstract
Pyranose oxidase and pyranosone dehydratase (aldos-2-ulose dehydratase), enzymes which convert in coupled reactions D-glucose to beta-pyrone cortalcerone, peaked coincidently during idiophasic growth of Phanerochaete chrysosporium under agitated conditions. The enzymes were purified from mycelial extracts of the fungus and separated from each other by hydrophobic interaction chromatography on Phenyl-Sepharose and Phenyl-Superose. Two pyranosone dehydratase activity peaks, PD I and PD II, were resolved. The major PD I fraction, consisting about 74% of the total dehydratase activity, was further purified by anion exchange chromatography on Mono Q to yield apparently pure enzyme as judged by SDS-PAGE and gel filtration on Superose 12. Isoelectric focusing indicated microheterogeneity of the protein by the presence of at least five protein bands with pI 5.1-5.3. PD II had a pI of 5.75. Overall PD I purification was 60.7-fold with 50% yield. The enzyme acted on several osones (glycosuloses), with the preferred substrate being D-glucosone. D-Xylosone and 6-deoxy-D-glucosone were dehydrated at C-3-C-4 to give the corresponding 5-hydroxy-2,3-dioxoalcanals (4-deoxy-2,3-glycosdiuloses), new enzymatically produced sugar derivatives. The latter labile compounds were trapped as diphenylhydrazine or o-phenylenediamine derivatives and spectroscopically identified. The analogous D-glucosone dehydration product did not accumulate due to its further transformation. pH optimum of PD I activity was 6.0 and its pH stability was optimal at pH 7-11. The enzyme was sensitive to Me2+ chelating agents and some heavy metal ions (Hg2+, Cu2+).
DOI: 10.1007/BF00258142
PubMed: 8352649
Affiliations:
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Sedmera</name></author><author><name sortKey="Daniel, G" sort="Daniel, G" uniqKey="Daniel G" first="G" last="Daniel">G. Daniel</name></author><author><name sortKey="Kubatova, E" sort="Kubatova, E" uniqKey="Kubatova E" first="E" last="Kubátová">E. Kubátová</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1993">1993</date><idno type="RBID">pubmed:8352649</idno><idno type="pmid">8352649</idno><idno type="doi">10.1007/BF00258142</idno><idno type="wicri:Area/Main/Corpus">000E34</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000E34</idno><idno type="wicri:Area/Main/Curation">000E34</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000E34</idno><idno type="wicri:Area/Main/Exploration">000E34</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Pyranosone dehydratase from the basidiomycete Phanerochaete chrysosporium: improved purification, and identification of 6-deoxy-D-glucosone and D-xylosone reaction products.</title><author><name sortKey="Gabriel, J" sort="Gabriel, J" uniqKey="Gabriel J" first="J" last="Gabriel">J. Gabriel</name><affiliation wicri:level="3"><nlm:affiliation>Institute of Microbiology, Academy of Sciences of Czech Republic, Prague.</nlm:affiliation><country>République tchèque</country><placeName><settlement type="city">Prague</settlement><region type="région" nuts="2">Bohême centrale</region></placeName><wicri:orgArea>Institute of Microbiology, Academy of Sciences of Czech Republic</wicri:orgArea></affiliation></author><author><name sortKey="Volc, J" sort="Volc, J" uniqKey="Volc J" first="J" last="Volc">J. Volc</name></author><author><name sortKey="Sedmera, P" sort="Sedmera, P" uniqKey="Sedmera P" first="P" last="Sedmera">P. Sedmera</name></author><author><name sortKey="Daniel, G" sort="Daniel, G" uniqKey="Daniel G" first="G" last="Daniel">G. Daniel</name></author><author><name sortKey="Kubatova, E" sort="Kubatova, E" uniqKey="Kubatova E" first="E" last="Kubátová">E. Kubátová</name></author></analytic><series><title level="j">Archives of microbiology</title><idno type="ISSN">0302-8933</idno><imprint><date when="1993" type="published">1993</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (enzymology)</term><term>Carbohydrate Dehydrogenases (biosynthesis)</term><term>Chelating Agents (pharmacology)</term><term>Chromatography, Ion Exchange (MeSH)</term><term>Deoxyglucose (analogs & derivatives)</term><term>Deoxyglucose (biosynthesis)</term><term>Deoxyglucose (metabolism)</term><term>Electrophoresis, Polyacrylamide Gel (MeSH)</term><term>Enzyme Stability (MeSH)</term><term>Hot Temperature (MeSH)</term><term>Hydro-Lyases (biosynthesis)</term><term>Hydro-Lyases (chemistry)</term><term>Hydro-Lyases (isolation & purification)</term><term>Hydro-Lyases (metabolism)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Isoelectric Focusing (MeSH)</term><term>Ketoses (biosynthesis)</term><term>Ketoses (metabolism)</term><term>Substrate Specificity (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Basidiomycota (enzymologie)</term><term>Carbohydrate dehydrogenases (biosynthèse)</term><term>Chromatographie d'échange d'ions (MeSH)</term><term>Chélateurs (pharmacologie)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Cétoses (sucres) (biosynthèse)</term><term>Cétoses (sucres) (métabolisme)</term><term>Désoxyglucose (analogues et dérivés)</term><term>Désoxyglucose (biosynthèse)</term><term>Désoxyglucose (métabolisme)</term><term>Focalisation isoélectrique (MeSH)</term><term>Hydro-lyases (biosynthèse)</term><term>Hydro-lyases (composition chimique)</term><term>Hydro-lyases (isolement et purification)</term><term>Hydro-lyases (métabolisme)</term><term>Spécificité du substrat (MeSH)</term><term>Stabilité enzymatique (MeSH)</term><term>Température élevée (MeSH)</term><term>Électrophorèse sur gel de polyacrylamide (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Deoxyglucose</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Carbohydrate Dehydrogenases</term><term>Deoxyglucose</term><term>Hydro-Lyases</term><term>Ketoses</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Hydro-Lyases</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Désoxyglucose</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Carbohydrate dehydrogenases</term><term>Cétoses (sucres)</term><term>Désoxyglucose</term><term>Hydro-lyases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Hydro-lyases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Basidiomycota</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Hydro-Lyases</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Hydro-lyases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Deoxyglucose</term><term>Hydro-Lyases</term><term>Ketoses</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cétoses (sucres)</term><term>Désoxyglucose</term><term>Hydro-lyases</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Chélateurs</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Chelating Agents</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Chromatography, Ion Exchange</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Enzyme Stability</term><term>Hot Temperature</term><term>Hydrogen-Ion Concentration</term><term>Isoelectric Focusing</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chromatographie d'échange d'ions</term><term>Concentration en ions d'hydrogène</term><term>Focalisation isoélectrique</term><term>Spécificité du substrat</term><term>Stabilité enzymatique</term><term>Température élevée</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Pyranose oxidase and pyranosone dehydratase (aldos-2-ulose dehydratase), enzymes which convert in coupled reactions D-glucose to beta-pyrone cortalcerone, peaked coincidently during idiophasic growth of Phanerochaete chrysosporium under agitated conditions. The enzymes were purified from mycelial extracts of the fungus and separated from each other by hydrophobic interaction chromatography on Phenyl-Sepharose and Phenyl-Superose. Two pyranosone dehydratase activity peaks, PD I and PD II, were resolved. The major PD I fraction, consisting about 74% of the total dehydratase activity, was further purified by anion exchange chromatography on Mono Q to yield apparently pure enzyme as judged by SDS-PAGE and gel filtration on Superose 12. Isoelectric focusing indicated microheterogeneity of the protein by the presence of at least five protein bands with pI 5.1-5.3. PD II had a pI of 5.75. Overall PD I purification was 60.7-fold with 50% yield. The enzyme acted on several osones (glycosuloses), with the preferred substrate being D-glucosone. D-Xylosone and 6-deoxy-D-glucosone were dehydrated at C-3-C-4 to give the corresponding 5-hydroxy-2,3-dioxoalcanals (4-deoxy-2,3-glycosdiuloses), new enzymatically produced sugar derivatives. The latter labile compounds were trapped as diphenylhydrazine or o-phenylenediamine derivatives and spectroscopically identified. The analogous D-glucosone dehydration product did not accumulate due to its further transformation. pH optimum of PD I activity was 6.0 and its pH stability was optimal at pH 7-11. The enzyme was sensitive to Me2+ chelating agents and some heavy metal ions (Hg2+, Cu2+).</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8352649</PMID><DateCompleted><Year>1993</Year><Month>09</Month><Day>10</Day></DateCompleted><DateRevised><Year>2019</Year><Month>09</Month><Day>04</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0302-8933</ISSN><JournalIssue CitedMedium="Print"><Volume>160</Volume><Issue>1</Issue><PubDate><Year>1993</Year></PubDate></JournalIssue><Title>Archives of microbiology</Title><ISOAbbreviation>Arch Microbiol</ISOAbbreviation></Journal><ArticleTitle>Pyranosone dehydratase from the basidiomycete Phanerochaete chrysosporium: improved purification, and identification of 6-deoxy-D-glucosone and D-xylosone reaction products.</ArticleTitle><Pagination><MedlinePgn>27-34</MedlinePgn></Pagination><Abstract><AbstractText>Pyranose oxidase and pyranosone dehydratase (aldos-2-ulose dehydratase), enzymes which convert in coupled reactions D-glucose to beta-pyrone cortalcerone, peaked coincidently during idiophasic growth of Phanerochaete chrysosporium under agitated conditions. The enzymes were purified from mycelial extracts of the fungus and separated from each other by hydrophobic interaction chromatography on Phenyl-Sepharose and Phenyl-Superose. Two pyranosone dehydratase activity peaks, PD I and PD II, were resolved. The major PD I fraction, consisting about 74% of the total dehydratase activity, was further purified by anion exchange chromatography on Mono Q to yield apparently pure enzyme as judged by SDS-PAGE and gel filtration on Superose 12. Isoelectric focusing indicated microheterogeneity of the protein by the presence of at least five protein bands with pI 5.1-5.3. PD II had a pI of 5.75. Overall PD I purification was 60.7-fold with 50% yield. The enzyme acted on several osones (glycosuloses), with the preferred substrate being D-glucosone. D-Xylosone and 6-deoxy-D-glucosone were dehydrated at C-3-C-4 to give the corresponding 5-hydroxy-2,3-dioxoalcanals (4-deoxy-2,3-glycosdiuloses), new enzymatically produced sugar derivatives. The latter labile compounds were trapped as diphenylhydrazine or o-phenylenediamine derivatives and spectroscopically identified. The analogous D-glucosone dehydration product did not accumulate due to its further transformation. pH optimum of PD I activity was 6.0 and its pH stability was optimal at pH 7-11. The enzyme was sensitive to Me2+ chelating agents and some heavy metal ions (Hg2+, Cu2+).</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gabriel</LastName><ForeName>J</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Institute of Microbiology, Academy of Sciences of Czech Republic, Prague.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Volc</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Sedmera</LastName><ForeName>P</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Daniel</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Kubátová</LastName><ForeName>E</ForeName><Initials>E</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Arch Microbiol</MedlineTA><NlmUniqueID>0410427</NlmUniqueID><ISSNLinking>0302-8933</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002614">Chelating Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007661">Ketoses</NameOfSubstance></Chemical><Chemical><RegistryNumber>26188-06-7</RegistryNumber><NameOfSubstance UI="C067906">threo-pentos-2-ulose</NameOfSubstance></Chemical><Chemical><RegistryNumber>54166-09-5</RegistryNumber><NameOfSubstance UI="C082558">6-deoxyglucosone</NameOfSubstance></Chemical><Chemical><RegistryNumber>9G2MP84A8W</RegistryNumber><NameOfSubstance UI="D003847">Deoxyglucose</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D002237">Carbohydrate Dehydrogenases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.3.10</RegistryNumber><NameOfSubstance UI="C022489">pyranose oxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.2.1.-</RegistryNumber><NameOfSubstance UI="D006836">Hydro-Lyases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.2.1.-</RegistryNumber><NameOfSubstance UI="C082557">pyranosone dehydratase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CitationSubset>S</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002237" MajorTopicYN="N">Carbohydrate Dehydrogenases</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002614" MajorTopicYN="N">Chelating Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002852" MajorTopicYN="N">Chromatography, Ion Exchange</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003847" MajorTopicYN="N">Deoxyglucose</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006358" MajorTopicYN="N">Hot Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006836" MajorTopicYN="N">Hydro-Lyases</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007525" MajorTopicYN="N">Isoelectric Focusing</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007661" MajorTopicYN="N">Ketoses</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1993</Year><Month>1</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1993</Year><Month>1</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1993</Year><Month>1</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8352649</ArticleId><ArticleId IdType="doi">10.1007/BF00258142</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Anal Biochem. 1972 Aug;48(2):422-7</Citation><ArticleIdList><ArticleId IdType="pubmed">4115981</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 1970 Aug 15;227(5259):680-5</Citation><ArticleIdList><ArticleId IdType="pubmed">5432063</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1979 Mar 25;254(6):2132-7</Citation><ArticleIdList><ArticleId IdType="pubmed">422572</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1966 Feb;55(2):388-93</Citation><ArticleIdList><ArticleId IdType="pubmed">5328727</ArticleId></ArticleIdList></Reference><Reference><Citation>Carbohydr Res. 1992 Jul 20;232(1):59-75</Citation><ArticleIdList><ArticleId IdType="pubmed">1423351</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>République tchèque</li></country><region><li>Bohême centrale</li></region><settlement><li>Prague</li></settlement></list><tree><noCountry><name sortKey="Daniel, G" sort="Daniel, G" uniqKey="Daniel G" first="G" last="Daniel">G. Daniel</name><name sortKey="Kubatova, E" sort="Kubatova, E" uniqKey="Kubatova E" first="E" last="Kubátová">E. Kubátová</name><name sortKey="Sedmera, P" sort="Sedmera, P" uniqKey="Sedmera P" first="P" last="Sedmera">P. Sedmera</name><name sortKey="Volc, J" sort="Volc, J" uniqKey="Volc J" first="J" last="Volc">J. Volc</name></noCountry><country name="République tchèque"><region name="Bohême centrale"><name sortKey="Gabriel, J" sort="Gabriel, J" uniqKey="Gabriel J" first="J" last="Gabriel">J. Gabriel</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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